β amyloid (1 40), fam labeled

β-Amyloid (1-40), FAM-labeled TFA is a FAM fluorescently-labelled?β-Amyloid (1-40) peptide (λ ex =?492?nm and λ em =?518?nm) [1] .

β-Amyloid (1-40), FAM-labeled, is a β-Amyloid (1-40) peptide tagged with a FAM fluorescent label, exhibiting an excitation wavelength (λ ex) of 492 nm and an emission wavelength (λ em) of 518 nm.

Amyloid β Peptide (42-1)(human) acetate is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human) acetate is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

β-Amyloid (1-42), acetate (human) is a peptide consisting of 42 amino acids that is part of β-Amyloid and is commonly used in Alzheimer's disease modeling.

β-amyloid 1-11 acetate is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.

β-Amyloid (1-16) rat is a fragment of the metal-binding domain of the amyloid beta (Abeta) peptide. It contains three amino acid substitutions that distinguish it from its human counterpart, conferring reduced susceptibility to Alzheimer's disease-like neurodegeneration in rats and mice [1].

NEP(1-40) TFA is a peptide antagonist of the Nogo-66 receptor (NgR), which mitigates the shift in microglial morphology distributions due to injury by attenuating myelin-derived inhibition [1].

β-Amyloid (1-40), England mutation, is a biologically active peptide with a histidine (His) to arginine (Arg) substitution at position 6, known to enhance oligomerization kinetics that serve as fibril seeds and increase neurotoxicity in cultured neurons. This alteration is one of several mutations in the beta-amyloid precursor gene implicated in autosomal dominant Alzheimer's Disease across multiple kindreds.

(Gln22,Asn23)-Amyloid β-Protein (1-40) is a peptide employed in the study of Cerebral Amyloid Angiopathy Mutations [1].

β-Amyloid (29-40) is a fragment of Amyloid-β peptide.Alzheimer's beta amyloid peptide (29-40/42) C-terminal fragments have physical and chemical properties related to those of fusion peptides of viral proteins. The fusion of liposomes can be induced by th

[Arg6]-β-Amyloid (1-42), England mutation, is a biologically active peptide associated with autosomal dominant Alzheimer's Disease in various kindreds. The English (H6R) mutation disrupts H6 interactions due to several mutations in the beta-amyloid precursor gene.

(Pyr11)-Amyloid β-Protein (11-40) (Aβ11pE-40), a peptide, is utilized in Alzheimer's disease research [1].

Anionic interaction of Beta-amyloid (1-11) with Factor XII is suspected to cause massive activation of the C4 (complement 4) system in the cerebrospinal fluid of Alzheimer’s disease patients.

Atrial Natriuretic Peptide (1-28), human, porcine, Biotin-labeled, is one of three mammalian natriuretic peptides (NPs) that exerts endocrine effects on fluid homeostasis and blood pressure. Atrial Natriuretic Peptide holds promise for cardiovascular diseases research.

Amyloid beta-protein(1-40) Arctic variant (Ab40ARC (E22G)), featuring a glycine at position 22 (Gly22), is a peptide utilized in Alzheimer's disease research [1].

Peptide fragment corresponding to residues 1 - 40 of Nogo-66, the domain of the myelin protein Nogo that inhibits axonal outgrowth. Acts as a competitive antagonist at the Nogo-66 receptor (NgR); blocks Nogo-66- and CNS myelin-induced inhibition of axonal

FITC-β-Ala-Amyloid β-Protein (1-42) ammonium, a fluorescein isothiocyanate (FITC)-tagged monomer peptide of Aβ1-42, is instrumental in Alzheimer’s disease pathogenesis [1].

Amyloid (1-42), rat is a polypeptide composed of 42 amino acids. It is toxic to hippocampal slices and can be used in the study of alzheimer's disease.

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide exhibiting increased aggregation propensity and fibril toxicity. This mutation involves the substitution of Aspartic acid (Asp) at position 23 with Asparagine (Asn), contributing to autosomal dominant Alzheimer's Disease in various kindreds due to its association with severe cerebral amyloid beta-protein angiopathy (CAA). Specifically, the mutation is a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

[Asn23] β-Amyloid (1-40), Iowa mutation, is a biologically active peptide associated with autosomal dominant Alzheimer's Disease in multiple families. This specific mutation involves the substitution of Asp 23 with Asn, leading to severe cerebral amyloid beta-protein angiopathy (CAA). Individuals with this mutation exhibit a missense alteration in the APP gene at position 694, which results in the mutated β-amyloid peptide aggregating more quickly and forming toxic fibrils.

β-Amyloid (42-1), human is the inactive form of Amyloid β Peptide (1-42) which plays a key role in the pathogenesis of Alzheimer disease.

Biotin-β-Amyloid (1-42), human TFA, also known as Biotin-Amyloid β-Peptide (1-42) (human) TFA, is a biotin-labeled 42-amino acid peptide implicated in the pathogenesis of Alzheimer's disease [1].

FAM-labeled Bid BH3 (80-99) is a biologically active peptide featuring a 5-FAM label at its N-terminus.

BAD (103-127) (human), FAM-labeled, is a FAM-labeled 25-mer peptide derived from the BH3 domain of human BAD. This peptide can antagonize the function of Bcl-xL [1].

Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42), a peptide fragment derived from amyloid β-protein (Aβ), plays a pivotal role in Alzheimer's disease research [1].

(Nle35)-Amyloid β-Protein (1-42) ammonium is a peptide.

Rat form of the beta-Amyloid (1-40) peptide

β-Amyloid (1-16) is an amyloidogenic protein fragment with a sequence derived from β-amyloid. It exhibits the ability to bind to metal ions, indicating its involvement in metal-binding processes. β-Amyloid, a peptide, is responsible for the formation of amyloid plaques in the brains of individuals affected by Alzheimer's disease (AD).

β-Amyloid (1-15) (Amyloid β-Protein (1-15)) is a fragment of β-amyloid protein used in the study of Alzheimer's disease.

β-Amyloid (1-40) TFA, a principal protein in plaques observed in the brains of Alzheimer's disease patients [1], is pivotal in research focused on this neurodegenerative disorder.

β-Amyloid (42-1), human TFA, a 42-amino acid peptide, represents the inactive form of Amyloid β Peptide (1-42) and is pivotal in the development of Alzheimer's disease [1].

(Gly22)-Amyloid β-Protein (1-42), a peptide fragment of Amyloid β-Protein (Aβ), plays a crucial role in Alzheimer's disease by forming the main component of both vascular and parenchymal amyloid deposits. The mutation from Glu22 to Gly22 in Aβ is known to enhance aggregation [1] [2].

'(Lys22)-Amyloid β-Protein (1-42) represents a mutation of the wild-type (WT) Amyloid β-Protein (1-42) peptide [1].'

Beta-Amyloid(1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. This peptide is amino acids 1 to 14 fragment of Beta-Amyloid peptide.

β-Amyloid (1-42), human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows the effects of cytotoxicity on acute hippocampal slices, and has been used in studies of alzheimer's disease.

This synthetic peptide consists of amino acids 1 to 17 of beta amyloid protein. This peptide can be employed in beta amyloid solubility studies.

β-Amyloid (33-40) is a peptide comprising amino acids 33 to 40 of the beta-amyloid protein.

β-Amyloid (1-43)(human) TFA exhibits greater aggregation tendencies and heightened toxicity compared to its well-established counterpart, Aβ1-42. Additionally, this compound demonstrates associations with both sAPPα and sAPPβ. It has the potential to serve as an additional biomarker for Alzheimer’s disease (AD), complementing existing markers [1].

Endothelin 1 (swine, human), Alexa Fluor 488-labeled, is a synthetic peptide corresponding to the sequence of human and swine Endothelin 1, a powerful endogenous vasoconstrictor, and is tagged with Alexa Fluor 488 for fluorescence. This compound operates via two receptor types, ET A and ET B [1].

Biotinyl-Ahx-Amyloid β-Protein (1-42) ammonium is an N-terminally biotin-tagged form of Amyloid β-Protein (1-42), which constitutes the main component of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

(Met(O2)35)-Amyloid β-Protein (1-42) is a peptide [1] .

(Met(O)35)-Amyloid β-Protein (1-42) represents the oxidized form of Methionine 35 in Aβ42, capable of producing an oligomer size distribution akin to that of Aβ40. This compound is utilized in Alzheimer’s disease (AD) research [1].

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), demonstrates increased fibrillogenic and pathogenic characteristics [1].

β-Amyloid (1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. β-Amyloid (1-14),mouse,rat is produced through the proteolytic processing of a transmembrane protein, amyloid precursor protein (APP), by β- and γ-secretases. β-Amyloid (1-14),mouse,rat accumulation in the brain is proposed to be an early toxic event in the pathogenesis of Alzheimer’s disease, which is the most common form of dementia associated with plaques and tangles in the brain[1]. [1]. Chen GF, et al. Amyloid beta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin. 2017 Sep;38(9):1205-1235.

β-Amyloid (1-38), derived from mice and rats, is a chemical compound comprising 38 amino acids, specifically residues 1-38 of the Aβ peptide. Notably, it serves as the primary constituent of amyloid plaques associated with Alzheimer's disease.

This is an N-terminal fragment of beta amyloid. It consists of amino acid residues 1 to 9. Truncated beta amyloid peptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly. This is attributed to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Notably, amyloid β-protein serves as the principal constituent of amyloid deposits found in both the vascular system and brain parenchyma in Alzheimer's disease [1] [2].

(D-Asp1)-Amyloid β-Protein (1-42), a peptide fragment of amyloid β-protein (Aβ), serves as the primary constituent of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

Biotin-β-Amyloid (17-40) is a biotinylated amyloid-ß-(1-40) peptide with a label at the N-terminal, constituting a 24-residue fragment resulting from the post-translational processing of amyloid precursor protein (APP) [1].

β-Amyloid (1-42), (rat/mouse) (TFA) is a peptide fragment consisting of 42 amino acids that can be used to study Alzheimer's disease.